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    On the cover
    The dynamin-related GTPase Drp1 (green) localizes in foci where it cleaves the mitochondrial network (red). Otera et al. demonstrate that the protein Mff is required for Drp1 recruitment and mitochondrial fission in mammalian cells. Image © 2010 Hidenori Otera.
    See page 1141.

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ISSN 0021-9525
EISSN 1540-8140
In this Issue

In This Issue

In Focus

Pair of studies clarifies how organelles attract enzymes that promote their fission.

People & Ideas

Rhoades studies protein folding and binding using single-molecule fluorescence techniques.

Review

The cell biology of disease

Report

Ino80 facilitates restoration of nucleosome structure during NER-mediated repair of UV-induced lesions.

The mitotic checkpoint protein Mad2 halts cell division by interfering with MKlp2-mediated relocation of the chromosome passenger complex from centromeres to the mitotic spindle.

Disruption of vesicle trafficking results in distortion of nuclear shape and increased nuclear envelope surface area but doesn’t alter the nuclear/cell volume ratio.

A conserved γ-tubulin complex–binding domain in CDK5RAP2 stimulates the microtubule-nucleating activity of γ-TuRC.

Article

Lte1 interacts with and inhibits the small GTPases Ras and Bud1, blocking polarization until mitosis is complete.

ER stress signaling involving calcium and CaMKII induces NADPH oxidase and oxidative stress, which amplify CHOP-mediated apoptosis via PKR activation.

Structural and functional studies of the Mdv1 dimer reveal how this mitochondria-associated adaptor protein orients and stabilizes the assembly of dynamins on membranes to promote mitochondrial fission.

Localization of the dynamin-related GTPase Drp1 to mitochondria relies on the mitochondrial fission factor Mff.

Phosphorylation of the muscle-specific formin splice variant FHOD3 by CK2 regulates its stability, myofibril targeting, and myofibril integrity.

AP-3 concentrates proteins within large dense-core vesicles to promote regulated exocytosis.

Changes in protein tyrosine phosphatase 1B expression affect duration and amplitude of EphA3 phosphorylation and cell surface concentration.

Rather than passively binding ligands via immunoreceptors, macrophages capture particles by repeated extension of actin-rich protrusions.

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